Eliminative Cleavage of Pectin and of Oligogalacturonide Methyl Esters by Pectin Trans-eliminase.
نویسندگان
چکیده
In the preceding paper (1) a method was described for the purification of the extracellular pectin trans-eliminase of Aspergillus jonsecaeus. The enzyme was purified by a three-step procedure to the point at which other pectic enzymes and cellulase were no longer detectable. The effects of pH, of Na+, Mg++, and Ca++ ions, and of a few anions on the activity of the enzyme were also reported. In the present paper an account is given of the course of action of pectin trans-eliminase on pectin and on certain oligogalacturonide methyl esters. The products of these reactions have been analyzed by paper chromatography.
منابع مشابه
Purification and Certain Properties of Pectin Trans-eliminase from Aspergillus Fonsecaeus.
In 1960 Albersheim, Neukom, and Deuel (1) reported on an enzyme present in a commercial pectic enzyme preparation (Pectin01 RlO, Rohm and Haas Company, Philadelphia) that degraded the a, 1 + 4-glycokidic bonds in pectin by a trans elimination of the proton on the 5th carbon atom of an anhydromethyl galacturonate unit with the oxygen of the adjacent glycosidic bond. Cleavage of the bonds in pect...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 239 شماره
صفحات -
تاریخ انتشار 1964